DAAA_BACSU
ID DAAA_BACSU Reviewed; 282 AA.
AC O07597;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=D-alanine aminotransferase;
DE EC=2.6.1.21;
DE AltName: Full=D-amino acid aminotransferase;
DE AltName: Full=D-amino acid transaminase;
DE Short=DAAT;
DE AltName: Full=D-aspartate aminotransferase;
GN Name=dat; Synonyms=yheM; OrderedLocusNames=BSU09670;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Acts on the D-isomers of alanine, leucine, aspartate,
CC glutamate, aminobutyrate, norvaline and asparagine. The enzyme
CC transfers an amino group from a substrate D-amino acid to the pyridoxal
CC phosphate cofactor to form pyridoxamine and an alpha-keto acid in the
CC first half-reaction. The second half-reaction is the reverse of the
CC first, transferring the amino group from the pyridoxamine to a second
CC alpha-keto acid to form the product D-amino acid via a ping-pong
CC mechanism. This is an important process in the formation of D-alanine
CC and D-glutamate, which are essential bacterial cell wall components (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + D-alanine = D-glutamate + pyruvate;
CC Xref=Rhea:RHEA:15869, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:57416; EC=2.6.1.21;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; Y14082; CAA74512.1; -; Genomic_DNA.
DR EMBL; Y14080; CAA74451.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12806.1; -; Genomic_DNA.
DR PIR; E69829; E69829.
DR RefSeq; NP_388848.1; NC_000964.3.
DR RefSeq; WP_003233305.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07597; -.
DR SMR; O07597; -.
DR STRING; 224308.BSU09670; -.
DR jPOST; O07597; -.
DR PaxDb; O07597; -.
DR PRIDE; O07597; -.
DR EnsemblBacteria; CAB12806; CAB12806; BSU_09670.
DR GeneID; 939759; -.
DR KEGG; bsu:BSU09670; -.
DR PATRIC; fig|224308.179.peg.1040; -.
DR eggNOG; COG0115; Bacteria.
DR InParanoid; O07597; -.
DR OMA; RGFQFAD; -.
DR PhylomeDB; O07597; -.
DR BioCyc; BSUB:BSU09670-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR GO; GO:0046437; P:D-amino acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019478; P:D-amino acid catabolic process; ISS:UniProtKB.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR005784; D_amino_transT.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01121; D_amino_aminoT; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..282
FT /note="D-alanine aminotransferase"
FT /id="PRO_0000103249"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 50
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 144
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 282 AA; 31182 MW; 49D5B75E5DF7DEC1 CRC64;
MKVLVNGRLI GRSEASIDLE DRGYQFGDGI YEVIRVYKGV LFGLREHAER FFRSAAEIGI
SLPFSIEDLE WDLQKLVQEN AVSEGAVYIQ TTRGVAPRKH QYEAGLEPQT TAYTFTVKKP
EQEQAYGVAA ITDEDLRWLR CDIKSLNLLY NVMTKQRAYE AGAFEAILLR DGVVTEGTSS
NVYAVINGTV RTHPANRLIL NGITRMNILG LIEKNGIKLD ETPVSEEELK QAEEIFISST
TAEIIPVVTL DGQSIGSGKP GPVTKQLQAA FQESIQQAAS IS
